ID GGA1_HUMAN Reviewed; 639 AA. AC Q9UJY5; A8K3D3; B0QYR7; Q5R3N1; Q5TG07; Q6IC75; Q86YA9; Q8NCS6; Q9BW94; AC Q9UG00; Q9UGW0; Q9UGW1; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 230. DE RecName: Full=ADP-ribosylation factor-binding protein GGA1; DE AltName: Full=Gamma-adaptin-related protein 1; DE AltName: Full=Golgi-localized, gamma ear-containing, ARF-binding protein 1; GN Name=GGA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10749927; DOI=10.1091/mbc.11.4.1241; RA Boman A.L., Zhang C.-J., Zhu X., Kahn R.A.; RT "A family of ADP-ribosylation factor effectors that can alter transport RT through the trans-Golgi."; RL Mol. Biol. Cell 11:1241-1255(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Heart; RX PubMed=10747089; DOI=10.1083/jcb.149.1.81; RA Dell'Angelica E.C., Puertollano R., Mullins C., Aguilar R.C., Vargas J.D., RA Hartnell L.M., Bonifacino J.S.; RT "GGAs: a family of ADP ribosylation factor-binding proteins related to RT adaptors and associated with the Golgi complex."; RL J. Cell Biol. 149:81-94(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10747088; DOI=10.1083/jcb.149.1.67; RA Hirst J., Lui W.W.Y., Bright N.A., Totty N., Seaman M.N.J., Robinson M.S.; RT "A family of proteins with gamma-adaptin and VHS domains that facilitate RT trafficking between the trans-Golgi network and the vacuole/lysosome."; RL J. Cell Biol. 149:67-80(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 275-639 (ISOFORMS 1/2/3). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-639 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP INTERACTION WITH SYNRG. RX PubMed=10814529; DOI=10.1006/bbrc.2000.2700; RA Takatsu H., Yoshino K., Nakayama K.; RT "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA RT proteins that interact with gamma-synergin."; RL Biochem. Biophys. Res. Commun. 271:719-725(2000). RN [11] RP INTERACTION WITH CLATHRIN, FUNCTION, MUTAGENESIS OF 356-LEU--GLU-360, AND RP DOMAIN. RX PubMed=11301005; DOI=10.1016/s0092-8674(01)00299-9; RA Puertollano R., Randazzo P.A., Presley J.F., Hartnell L.M., RA Bonifacino J.S.; RT "The GGAs promote ARF-dependent recruitment of clathrin to the TGN."; RL Cell 105:93-102(2001). RN [12] RP INTERACTION WITH SORT1; LRP3 AND IGF2R. RX PubMed=11390366; DOI=10.1074/jbc.c100218200; RA Takatsu H., Katoh Y., Shiba Y., Nakayama K.; RT "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation RT factor-binding (GGA) proteins interact with acidic dileucine sequences RT within the cytoplasmic domains of sorting receptors through their RT Vps27p/Hrs/STAM (VHS) domains."; RL J. Biol. Chem. 276:28541-28545(2001). RN [13] RP INTERACTION WITH M6PR AND IGF2R. RX PubMed=11387475; DOI=10.1126/science.1060750; RA Puertollano R., Aguilar R.C., Gorshkova I., Crouch R.J., Bonifacino J.S.; RT "Sorting of mannose 6-phosphate receptors mediated by the GGAs."; RL Science 292:1712-1716(2001). RN [14] RP INTERACTION WITH ARF1; ARF5 AND ARF6. RX PubMed=11950392; DOI=10.1042/bj20020428; RA Takatsu H., Yoshino K., Toda K., Nakayama K.; RT "GGA proteins associate with Golgi membranes through interaction between RT their GGAH domains and ADP-ribosylation factors."; RL Biochem. J. 365:369-378(2002). RN [15] RP INTERACTION WITH SORT1 AND SORL1. RX PubMed=11821067; DOI=10.1016/s0014-5793(01)03299-9; RA Jacobsen L., Madsen P., Nielsen M.S., Geraerts W.P.M., Gliemann J., RA Smit A.B., Petersen C.M.; RT "The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines RT minimum requirements for GGA binding."; RL FEBS Lett. 511:155-158(2002). RN [16] RP MUTAGENESIS OF ASN-92; SER-355; ASP-358 AND 361-LEU-MET-362, RP PHOSPHORYLATION AT SER-355, AND INTERACTION WITH IGF2R. RX PubMed=12060753; DOI=10.1073/pnas.082235699; RA Doray B., Bruns K., Ghosh P., Kornfeld S.A.; RT "Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an RT internal acidic cluster-dileucine motif."; RL Proc. Natl. Acad. Sci. U.S.A. 99:8072-8077(2002). RN [17] RP INTERACTION WITH BACE1. RX PubMed=14567678; DOI=10.1021/bi035199h; RA He X., Zhu G., Koelsch G., Rodgers K.K., Zhang X.C., Tang J.; RT "Biochemical and structural characterization of the interaction of memapsin RT 2 (beta-secretase) cytosolic domain with the VHS domain of GGA proteins."; RL Biochemistry 42:12174-12180(2003). RN [18] RP INTERACTION WITH RABEP1 AND RABGEF1. RX PubMed=12505986; DOI=10.1093/emboj/cdg015; RA Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S.; RT "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex."; RL EMBO J. 22:78-88(2003). RN [19] RP REGULATION BY PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PP2A. RX PubMed=12578827; DOI=10.1074/jbc.m212543200; RA Ghosh P., Kornfeld S.; RT "Phosphorylation-induced conformational changes regulate GGAs 1 and 3 RT function at the trans-Golgi network."; RL J. Biol. Chem. 278:14543-14549(2003). RN [20] RP INTERACTION WITH EPN4. RX PubMed=12538641; DOI=10.1083/jcb.200208023; RA Mills I.G., Praefcke G.J.K., Vallis Y., Peter B.J., Olesen L.E., RA Gallop J.L., Butler P.J.G., Evans P.R., McMahon H.T.; RT "EpsinR: an AP1/clathrin interacting protein involved in vesicle RT trafficking."; RL J. Cell Biol. 160:213-222(2003). RN [21] RP INTERACTION WITH GGA2 AND GGA3, AND SUBCELLULAR LOCATION. RX PubMed=14638859; DOI=10.1083/jcb.200308038; RA Ghosh P., Griffith J., Geuze H.J., Kornfeld S.; RT "Mammalian GGAs act together to sort mannose 6-phosphate receptors."; RL J. Cell Biol. 163:755-766(2003). RN [22] RP INTERACTION WITH CCDC91; P200 AND SYNRG, AND MUTAGENESIS OF ALA-563; RP VAL-564; VAL-570 AND LEU-572. RX PubMed=12808037; DOI=10.1091/mbc.e02-11-0735; RA Lui W.W.Y., Collins B.M., Hirst J., Motley A., Millar C., Schu P., RA Owen D.J., Robinson M.S.; RT "Binding partners for the COOH-terminal appendage domains of the GGAs and RT gamma-adaptin."; RL Mol. Biol. Cell 14:2385-2398(2003). RN [23] RP INTERACTION WITH UBC. RX PubMed=14660606; DOI=10.1074/jbc.m311702200; RA Shiba Y., Katoh Y., Shiba T., Yoshino K., Takatsu H., Kobayashi H., RA Shin H.-W., Wakatsuki S., Nakayama K.; RT "GAT (GGA and Tom1) domain responsible for ubiquitin binding and RT ubiquitination."; RL J. Biol. Chem. 279:7105-7111(2004). RN [24] RP INTERACTION WITH RABEP1; NECAP1; NECAP2 AND AFTPH. RX PubMed=14665628; DOI=10.1074/jbc.m311873200; RA Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.; RT "Definition of the consensus motif recognized by gamma-adaptin ear RT domains."; RL J. Biol. Chem. 279:8018-8028(2004). RN [25] RP INTERACTION WITH ARF1; RABEP1; UBC AND TSG101, MUTAGENESIS OF LEU-182; RP ASN-194; ILE-197; LYS-198; MET-200; ASP-204; MET-259; ARG-260; PHE-264; RP ALA-267; LEU-277; LEU-281 AND ASN-284, AND DOMAIN. RX PubMed=15143060; DOI=10.1074/jbc.m402183200; RA Mattera R., Puertollano R., Smith W.J., Bonifacino J.S.; RT "The trihelical bundle subdomain of the GGA proteins interacts with RT multiple partners through overlapping but distinct sites."; RL J. Biol. Chem. 279:31409-31418(2004). RN [26] RP SUBCELLULAR LOCATION. RX PubMed=15039775; DOI=10.1038/ncb1106; RA Puertollano R., Bonifacino J.S.; RT "Interactions of GGA3 with the ubiquitin sorting machinery."; RL Nat. Cell Biol. 6:244-251(2004). RN [27] RP FUNCTION. RX PubMed=15615712; DOI=10.1074/jbc.m411296200; RA He X., Li F., Chang W.P., Tang J.; RT "GGA proteins mediate the recycling pathway of memapsin 2 (BACE)."; RL J. Biol. Chem. 280:11696-11703(2005). RN [28] RP INTERACTION WITH AFTPH; HEATR5B AND SYNRG. RX PubMed=15758025; DOI=10.1091/mbc.e04-12-1077; RA Hirst J., Borner G.H., Harbour M., Robinson M.S.; RT "The aftiphilin/p200/gamma-synergin complex."; RL Mol. Biol. Cell 16:2554-2565(2005). RN [29] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BACE1. RX PubMed=15886016; DOI=10.1016/j.mcn.2005.03.014; RA Wahle T., Prager K., Raffler N., Haass C., Famulok M., Walter J.; RT "GGA proteins regulate retrograde transport of BACE1 from endosomes to the RT trans-Golgi network."; RL Mol. Cell. Neurosci. 29:453-461(2005). RN [30] RP INTERACTION WITH SORL1. RX PubMed=17855360; DOI=10.1074/jbc.m705073200; RA Schmidt V., Sporbert A., Rohe M., Reimer T., Rehm A., Andersen O.M., RA Willnow T.E.; RT "SorLA/LR11 regulates processing of amyloid precursor protein via RT interaction with adaptors GGA and PACS-1."; RL J. Biol. Chem. 282:32956-32964(2007). RN [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [32] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [34] RP INTERACTION WITH RNF11. RX PubMed=20676133; DOI=10.1038/onc.2010.294; RA Santonico E., Belleudi F., Panni S., Torrisi M.R., Cesareni G., RA Castagnoli L.; RT "Multiple modification and protein interaction signals drive the Ring RT finger protein 11 (RNF11) E3 ligase to the endosomal compartment."; RL Oncogene 29:5604-5618(2010). RN [35] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [36] RP INTERACTION WITH ARF6. RX PubMed=22522702; DOI=10.1038/emboj.2012.89; RA Makyio H., Ohgi M., Takei T., Takahashi S., Takatsu H., Katoh Y., Hanai A., RA Ueda T., Kanaho Y., Xie Y., Shin H.W., Kamikubo H., Kataoka M., RA Kawasaki M., Kato R., Wakatsuki S., Nakayama K.; RT "Structural basis for Arf6-MKLP1 complex formation on the Flemming body RT responsible for cytokinesis."; RL EMBO J. 31:2590-2603(2012). RN [37] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [38] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [40] RP FUNCTION, AND INTERACTION WITH ADRA2B. RX PubMed=27901063; DOI=10.1038/srep37921; RA Zhang M., Huang W., Gao J., Terry A.V., Wu G.; RT "Regulation of alpha2B-Adrenergic Receptor Cell Surface Transport by GGA1 RT and GGA2."; RL Sci. Rep. 6:37921-37921(2016). RN [41] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-147. RX PubMed=11859376; DOI=10.1038/415937a; RA Shiba T., Takatsu H., Nogi T., Matsugaki N., Kawasaki M., Igarashi N., RA Suzuki M., Kato R., Earnest T., Nakayama K., Wakatsuki S.; RT "Structural basis for recognition of acidic-cluster dileucine sequence by RT GGA1."; RL Nature 415:937-941(2002). RN [42] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 168-208 IN COMPLEX WITH MOUSE RP ARF1. RX PubMed=12679809; DOI=10.1038/nsb920; RA Shiba T., Kawasaki M., Takatsu H., Nogi T., Matsugaki N., Igarashi N., RA Suzuki M., Kato R., Nakayama K., Wakatsuki S.; RT "Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal RT protein transport."; RL Nat. Struct. Biol. 10:386-393(2003). RN [43] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-16 IN COMPLEX WITH CCDC91. RX PubMed=12858163; DOI=10.1038/nsb955; RA Collins B.M., Praefcke G.J., Robinson M.S., Owen D.J.; RT "Structural basis for binding of accessory proteins by the appendage domain RT of GGAs."; RL Nat. Struct. Biol. 10:607-613(2003). RN [44] {ECO:0007744|PDB:3G2S, ECO:0007744|PDB:3G2T, ECO:0007744|PDB:3G2U, ECO:0007744|PDB:3G2V, ECO:0007744|PDB:3G2W} RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-147 IN COMPLEX WITH SORL1 AND RP SORT1, INTERACTION WITH SORL1 AND SORT1, AND MUTAGENESIS OF SER-355. RX PubMed=20015111; DOI=10.1111/j.1600-0854.2009.01017.x; RA Cramer J.F., Gustafsen C., Behrens M.A., Oliveira C.L., Pedersen J.S., RA Madsen P., Petersen C.M., Thirup S.S.; RT "GGA autoinhibition revisited."; RL Traffic 11:259-273(2010). RN [45] RP VARIANTS [LARGE SCALE ANALYSIS] SER-239 AND ALA-484. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plays a role in protein sorting and trafficking between the CC trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent CC recruitment of clathrin to the TGN and binds ubiquitinated proteins and CC membrane cargo molecules with a cytosolic acidic cluster-dileucine CC (DXXLL) motif (PubMed:11301005, PubMed:15886016). Mediates export of CC the GPCR receptor ADRA2B to the cell surface (PubMed:27901063). CC Required for targeting PKD1:PKD2 complex from the trans-Golgi network CC to the cilium membrane (By similarity). Regulates retrograde transport CC of proteins such as phosphorylated form of BACE1 from endosomes to the CC trans-Golgi network (PubMed:15886016, PubMed:15615712). CC {ECO:0000250|UniProtKB:Q8R0H9, ECO:0000269|PubMed:11301005, CC ECO:0000269|PubMed:15615712, ECO:0000269|PubMed:15886016, CC ECO:0000269|PubMed:27901063}. CC -!- SUBUNIT: Monomer (Probable). Interacts with GGA2 and GGA3 CC (PubMed:14638859). Binds to clathrin and activated ARFs, including CC ARF1, ARF5 and ARF6 (PubMed:11301005, PubMed:11950392, PubMed:12679809, CC PubMed:15143060, PubMed:22522702). Interacts with RABEP1 CC (PubMed:12505986, PubMed:15143060, PubMed:14665628). Interacts with CC RABGEF1 (PubMed:12505986, PubMed:15143060). Interacts with the type-I CC membrane proteins LRP3, M6PR/CD-MPR and IGF2R/CI-MPR (PubMed:11390366, CC PubMed:11387475, PubMed:12060753). Interacts (via N-terminal VHS CC domain) with SORL1/sorLA and SORT1 (via C-terminal cytosolic domain) CC (PubMed:11821067, PubMed:17855360, PubMed:20015111). Interacts with CC EPN4 (PubMed:12538641). Interacts with CCDC91 (PubMed:12808037, CC PubMed:12858163). Interacts with HEATR5B/p200a (PubMed:12808037, CC PubMed:15758025). Interacts with SYNRG/gamma-synergin (PubMed:10814529, CC PubMed:12808037, PubMed:15758025). Interacts (via GAE doamin) with CC NECAP1 and NECAP2 (PubMed:14665628). Interacts (via GAE domain) with CC AFTPH/aftiphilin (PubMed:14665628, PubMed:15758025). Interacts with CC TSG101 and UBC (PubMed:14660606, PubMed:15143060). Interacts with RNF11 CC (PubMed:20676133). Interacts (via VHS domain) with BACE1 (via DXXLL CC motif); the interaction highly increases when BACE1 is phosphorylated CC at 'Ser-498' (PubMed:14567678, PubMed:15886016). Interacts with CNST CC (By similarity). Interacts with ADRA2B (PubMed:27901063). Interacts CC with ARL3; the interaction recruits, in collaboration with RABEP1, CC PKD1:PKD2 complex to trans-Golgi network and is required for ciliary CC targeting (By similarity). {ECO:0000250|UniProtKB:Q8R0H9, CC ECO:0000269|PubMed:10814529, ECO:0000269|PubMed:11301005, CC ECO:0000269|PubMed:11387475, ECO:0000269|PubMed:11390366, CC ECO:0000269|PubMed:11821067, ECO:0000269|PubMed:11950392, CC ECO:0000269|PubMed:12060753, ECO:0000269|PubMed:12505986, CC ECO:0000269|PubMed:12538641, ECO:0000269|PubMed:12679809, CC ECO:0000269|PubMed:12808037, ECO:0000269|PubMed:12858163, CC ECO:0000269|PubMed:14567678, ECO:0000269|PubMed:14638859, CC ECO:0000269|PubMed:14660606, ECO:0000269|PubMed:14665628, CC ECO:0000269|PubMed:15143060, ECO:0000269|PubMed:15758025, CC ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:17855360, CC ECO:0000269|PubMed:20015111, ECO:0000269|PubMed:20676133, CC ECO:0000269|PubMed:22522702, ECO:0000269|PubMed:27901063, ECO:0000305}. CC -!- INTERACTION: CC Q9UJY5; P56817: BACE1; NbExp=4; IntAct=EBI-447141, EBI-2433139; CC Q9UJY5; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-447141, EBI-747505; CC Q9UJY5; P13569: CFTR; NbExp=6; IntAct=EBI-447141, EBI-349854; CC Q9UJY5; O60941: DTNB; NbExp=4; IntAct=EBI-447141, EBI-740402; CC Q9UJY5; Q9UJY4: GGA2; NbExp=7; IntAct=EBI-447141, EBI-447646; CC Q9UJY5; Q9NZ52: GGA3; NbExp=4; IntAct=EBI-447141, EBI-447404; CC Q9UJY5; Q9NYZ3: GTSE1; NbExp=2; IntAct=EBI-447141, EBI-2511327; CC Q9UJY5; P11717: IGF2R; NbExp=9; IntAct=EBI-447141, EBI-1048580; CC Q9UJY5; P05412: JUN; NbExp=2; IntAct=EBI-447141, EBI-852823; CC Q9UJY5; Q7Z3U7: MON2; NbExp=2; IntAct=EBI-447141, EBI-358882; CC Q9UJY5; Q15276: RABEP1; NbExp=8; IntAct=EBI-447141, EBI-447043; CC Q9UJY5; Q9Y3C5: RNF11; NbExp=7; IntAct=EBI-447141, EBI-396669; CC Q9UJY5; Q92673: SORL1; NbExp=4; IntAct=EBI-447141, EBI-1171329; CC Q9UJY5; Q99523: SORT1; NbExp=2; IntAct=EBI-447141, EBI-1057058; CC Q9UJY5; P0CG47: UBB; NbExp=3; IntAct=EBI-447141, EBI-413034; CC Q9UJY5; P19328: Adra2b; Xeno; NbExp=3; IntAct=EBI-447141, EBI-21453893; CC Q9UJY5; P62331: Arf6; Xeno; NbExp=2; IntAct=EBI-447141, EBI-988682; CC Q9UJY5; O18973: RABGEF1; Xeno; NbExp=2; IntAct=EBI-447141, EBI-447376; CC Q9UJY5-4; P05067: APP; NbExp=3; IntAct=EBI-12108696, EBI-77613; CC Q9UJY5-4; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-12108696, EBI-747505; CC Q9UJY5-4; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-12108696, EBI-25836642; CC Q9UJY5-4; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-12108696, EBI-742953; CC Q9UJY5-4; O60941-5: DTNB; NbExp=3; IntAct=EBI-12108696, EBI-11984733; CC Q9UJY5-4; Q8WYH8: ING5; NbExp=3; IntAct=EBI-12108696, EBI-488533; CC Q9UJY5-4; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-12108696, EBI-1055254; CC Q9UJY5-4; A4D0Q3: KIAA1218; NbExp=3; IntAct=EBI-12108696, EBI-14308786; CC Q9UJY5-4; I6L9F6: NEFL; NbExp=3; IntAct=EBI-12108696, EBI-10178578; CC Q9UJY5-5; Q14114-3: LRP8; NbExp=3; IntAct=EBI-25903400, EBI-25832196; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:15886016}; Peripheral membrane protein. Endosome CC membrane {ECO:0000269|PubMed:15886016}; Peripheral membrane protein. CC Early endosome membrane {ECO:0000269|PubMed:15886016}; Peripheral CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q9UJY5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UJY5-2; Sequence=VSP_001744; CC Name=3; CC IsoId=Q9UJY5-3; Sequence=VSP_042806; CC Name=4; CC IsoId=Q9UJY5-4; Sequence=VSP_042809; CC Name=5; CC IsoId=Q9UJY5-5; Sequence=VSP_042807, VSP_042808; CC Name=6; CC IsoId=Q9UJY5-6; Sequence=VSP_057352; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC -!- DOMAIN: The VHS domain functions as a recognition module for sorting CC signals composed of an acidic cluster followed by two leucines (DXXLL CC motif). CC -!- DOMAIN: The GAT domain is responsible for interaction with ARF-GTP, UBC CC and RABEP1. Required for recruitment to the TGN it prevents ARF-GTP CC hydrolysis. {ECO:0000269|PubMed:15143060}. CC -!- DOMAIN: The unstructured hinge region contains clathrin-binding but no CC autoinhibitory (DXXLL) motifs. {ECO:0000269|PubMed:11301005}. CC -!- DOMAIN: The GAE domain binds accessory proteins regulating GGAs CC function. CC -!- PTM: Phosphorylated by CK2 and dephosphorylated by PP2A. CC Phosphorylation of GGA1 allows the internal DXXLL motif to bind the VHS CC domain and to inhibit the recognition of cargo signals. CC {ECO:0000269|PubMed:12060753}. CC -!- PTM: Ubiquitinated. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GGA protein family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF190862; AAF05707.1; -; mRNA. DR EMBL; AF218584; AAF42847.1; -; mRNA. DR EMBL; AF233521; AAF35393.1; -; mRNA. DR EMBL; CR456493; CAG30379.1; -; mRNA. DR EMBL; AK075256; BAC11501.1; -; mRNA. DR EMBL; AK122898; BAG53788.1; -; mRNA. DR EMBL; AK290548; BAF83237.1; -; mRNA. DR EMBL; AL035496; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471095; EAW60169.1; -; Genomic_DNA. DR EMBL; BC000538; AAH00538.2; -; mRNA. DR EMBL; BC010917; AAH10917.1; -; mRNA. DR EMBL; BC029388; AAH29388.1; -; mRNA. DR EMBL; BC044629; AAH44629.1; -; mRNA. DR EMBL; AL110219; CAB53679.1; -; mRNA. DR CCDS; CCDS13951.1; -. [Q9UJY5-1] DR CCDS; CCDS33643.1; -. [Q9UJY5-4] DR CCDS; CCDS54526.1; -. [Q9UJY5-3] DR CCDS; CCDS87022.1; -. [Q9UJY5-6] DR PIR; T14759; T14759. DR RefSeq; NP_001001560.1; NM_001001560.2. [Q9UJY5-4] DR RefSeq; NP_001166158.1; NM_001172687.1. DR RefSeq; NP_001166159.1; NM_001172688.1. [Q9UJY5-3] DR RefSeq; NP_037497.1; NM_013365.4. [Q9UJY5-1] DR RefSeq; XP_005261574.1; XM_005261517.3. DR RefSeq; XP_005261577.1; XM_005261520.1. DR RefSeq; XP_006724292.1; XM_006724229.1. [Q9UJY5-3] DR RefSeq; XP_011528424.1; XM_011530122.1. DR RefSeq; XP_016884249.1; XM_017028760.1. DR RefSeq; XP_016884250.1; XM_017028761.1. DR RefSeq; XP_016884251.1; XM_017028762.1. DR PDB; 1J2J; X-ray; 1.60 A; B=166-210. DR PDB; 1JWF; X-ray; 2.10 A; A=1-147. DR PDB; 1JWG; X-ray; 2.00 A; A/B=1-147. DR PDB; 1NA8; X-ray; 2.30 A; A/B=494-639. DR PDB; 1NAF; X-ray; 2.80 A; A=165-314. DR PDB; 1NWM; X-ray; 2.40 A; X=166-302. DR PDB; 1O3X; X-ray; 2.10 A; A=166-305. DR PDB; 1OM9; X-ray; 2.50 A; A/B=494-639. DR PDB; 1OXZ; X-ray; 2.80 A; A=141-326. DR PDB; 1PY1; X-ray; 2.60 A; A/B/C/D=2-157. DR PDB; 1UJJ; X-ray; 2.60 A; A/B=1-147. DR PDB; 1UJK; X-ray; 1.90 A; A/B=1-147. DR PDB; 1X79; X-ray; 2.41 A; A=210-302. DR PDB; 2DWX; X-ray; 2.55 A; A/B/C/D=507-639, P/Q=376-388. DR PDB; 2DWY; X-ray; 2.30 A; A/B/C/D=507-639. DR PDB; 3G2S; X-ray; 1.70 A; A/B=1-147. DR PDB; 3G2T; X-ray; 2.00 A; A/B=1-147. DR PDB; 3G2U; X-ray; 2.30 A; A/B=1-147. DR PDB; 3G2V; X-ray; 2.10 A; A/B=1-147. DR PDB; 3G2W; X-ray; 2.40 A; A/B=1-147, C/D=351-364. DR PDBsum; 1J2J; -. DR PDBsum; 1JWF; -. DR PDBsum; 1JWG; -. DR PDBsum; 1NA8; -. DR PDBsum; 1NAF; -. DR PDBsum; 1NWM; -. DR PDBsum; 1O3X; -. DR PDBsum; 1OM9; -. DR PDBsum; 1OXZ; -. DR PDBsum; 1PY1; -. DR PDBsum; 1UJJ; -. DR PDBsum; 1UJK; -. DR PDBsum; 1X79; -. DR PDBsum; 2DWX; -. DR PDBsum; 2DWY; -. DR PDBsum; 3G2S; -. DR PDBsum; 3G2T; -. DR PDBsum; 3G2U; -. DR PDBsum; 3G2V; -. DR PDBsum; 3G2W; -. DR AlphaFoldDB; Q9UJY5; -. DR SMR; Q9UJY5; -. DR BioGRID; 117540; 116. DR ELM; Q9UJY5; -. DR IntAct; Q9UJY5; 83. DR MINT; Q9UJY5; -. DR STRING; 9606.ENSP00000371175; -. DR TCDB; 9.B.278.1.2; the organellar-targeting adaptor protein complex (o-apc) family. DR GlyGen; Q9UJY5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UJY5; -. DR PhosphoSitePlus; Q9UJY5; -. DR BioMuta; GGA1; -. DR DMDM; 14548066; -. DR EPD; Q9UJY5; -. DR jPOST; Q9UJY5; -. DR MassIVE; Q9UJY5; -. DR MaxQB; Q9UJY5; -. DR PaxDb; 9606-ENSP00000341344; -. DR PeptideAtlas; Q9UJY5; -. DR ProteomicsDB; 66377; -. DR ProteomicsDB; 84692; -. [Q9UJY5-1] DR ProteomicsDB; 84693; -. [Q9UJY5-2] DR ProteomicsDB; 84694; -. [Q9UJY5-3] DR ProteomicsDB; 84695; -. [Q9UJY5-4] DR ProteomicsDB; 84696; -. [Q9UJY5-5] DR Pumba; Q9UJY5; -. DR Antibodypedia; 12029; 262 antibodies from 28 providers. DR DNASU; 26088; -. DR Ensembl; ENST00000325180.12; ENSP00000321288.8; ENSG00000100083.19. [Q9UJY5-4] DR Ensembl; ENST00000343632.9; ENSP00000341344.4; ENSG00000100083.19. [Q9UJY5-1] DR Ensembl; ENST00000381756.9; ENSP00000371175.5; ENSG00000100083.19. [Q9UJY5-6] DR Ensembl; ENST00000406772.5; ENSP00000385287.1; ENSG00000100083.19. [Q9UJY5-3] DR GeneID; 26088; -. DR KEGG; hsa:26088; -. DR MANE-Select; ENST00000343632.9; ENSP00000341344.4; NM_013365.5; NP_037497.1. DR UCSC; uc003atc.4; human. [Q9UJY5-1] DR AGR; HGNC:17842; -. DR CTD; 26088; -. DR DisGeNET; 26088; -. DR GeneCards; GGA1; -. DR HGNC; HGNC:17842; GGA1. DR HPA; ENSG00000100083; Tissue enhanced (testis). DR MIM; 606004; gene. DR neXtProt; NX_Q9UJY5; -. DR OpenTargets; ENSG00000100083; -. DR PharmGKB; PA28657; -. DR VEuPathDB; HostDB:ENSG00000100083; -. DR eggNOG; KOG1086; Eukaryota. DR GeneTree; ENSGT00940000156448; -. DR HOGENOM; CLU_015010_0_0_1; -. DR InParanoid; Q9UJY5; -. DR OMA; PDNYEPN; -. DR OrthoDB; 2917368at2759; -. DR PhylomeDB; Q9UJY5; -. DR TreeFam; TF318574; -. DR PathwayCommons; Q9UJY5; -. DR Reactome; R-HSA-8854214; TBC/RABGAPs. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR SignaLink; Q9UJY5; -. DR SIGNOR; Q9UJY5; -. DR BioGRID-ORCS; 26088; 9 hits in 1150 CRISPR screens. DR ChiTaRS; GGA1; human. DR EvolutionaryTrace; Q9UJY5; -. DR GeneWiki; GGA1; -. DR GenomeRNAi; 26088; -. DR Pharos; Q9UJY5; Tbio. DR PRO; PR:Q9UJY5; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q9UJY5; Protein. DR Bgee; ENSG00000100083; Expressed in pancreatic ductal cell and 195 other cell types or tissues. DR ExpressionAtlas; Q9UJY5; baseline and differential. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0010008; C:endosome membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA. DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro. DR GO; GO:0031267; F:small GTPase binding; IPI:CAFA. DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB. DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl. DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl. DR GO; GO:0008104; P:protein localization; IDA:UniProtKB. DR GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB. DR GO; GO:1903441; P:protein localization to ciliary membrane; IEA:Ensembl. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB. DR CDD; cd14239; GAT_GGA1_GGA2; 1. DR CDD; cd17009; VHS_GGA1; 1. DR DisProt; DP00314; -. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.58.160; -; 1. DR Gene3D; 1.25.40.90; -; 1. DR Gene3D; 2.60.40.1230; -; 1. DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig. DR InterPro; IPR013041; Clathrin_app_Ig-like_sf. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR008153; GAE_dom. DR InterPro; IPR004152; GAT_dom. DR InterPro; IPR038425; GAT_sf. DR InterPro; IPR027422; GGA1-3. DR InterPro; IPR041198; GGA_N-GAT. DR InterPro; IPR002014; VHS_dom. DR PANTHER; PTHR45905:SF4; ADP-RIBOSYLATION FACTOR-BINDING PROTEIN GGA1; 1. DR PANTHER; PTHR45905; GOLGI-LOCALIZED, GAMMA-ADAPTIN EAR CONTAINING, ARF BINDING PROTEIN; 1. DR Pfam; PF02883; Alpha_adaptinC2; 1. DR Pfam; PF03127; GAT; 1. DR Pfam; PF18308; GGA_N-GAT; 1. DR Pfam; PF00790; VHS; 1. DR SMART; SM00809; Alpha_adaptinC2; 1. DR SMART; SM00288; VHS; 1. DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1. DR SUPFAM; SSF48464; ENTH/VHS domain; 1. DR SUPFAM; SSF89009; GAT-like domain; 1. DR PROSITE; PS50180; GAE; 1. DR PROSITE; PS50909; GAT; 1. DR PROSITE; PS50179; VHS; 1. DR Genevisible; Q9UJY5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Endosome; Golgi apparatus; KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport; KW Ubl conjugation. FT CHAIN 1..639 FT /note="ADP-ribosylation factor-binding protein GGA1" FT /id="PRO_0000212680" FT DOMAIN 17..147 FT /note="VHS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218" FT DOMAIN 171..299 FT /note="GAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373" FT DOMAIN 510..631 FT /note="GAE" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093" FT REGION 114..274 FT /note="Interaction with ARF3" FT REGION 300..509 FT /note="Unstructured hinge" FT REGION 320..421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 434..492 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 358..362 FT /note="Autoinhibitory" FT COMPBIAS 369..393 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 434..478 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 185 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 355 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000305|PubMed:12060753" FT MOD_RES 418 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..73 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042806" FT VAR_SEQ 68 FT /note="T -> TVRRGEATIRPPPCDDTK (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15461802" FT /id="VSP_057352" FT VAR_SEQ 69..101 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_001744" FT VAR_SEQ 70..89 FT /note="LETCMKSCGKRFHDEVGKFR -> RRGEATIRPPPCDDTKGGQD (in FT isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042807" FT VAR_SEQ 90..639 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042808" FT VAR_SEQ 277..363 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042809" FT VARIANT 239 FT /note="G -> S (in a breast cancer sample; somatic mutation; FT dbSNP:rs765255006)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036522" FT VARIANT 484 FT /note="P -> A (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036523" FT MUTAGEN 92 FT /note="N->A: Abolishes interaction with IGF2R." FT /evidence="ECO:0000269|PubMed:12060753" FT MUTAGEN 182 FT /note="L->A: Abolishes interaction with ARF1, UBC and FT TSG101." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 194 FT /note="N->A: Abolishes interaction with ARF1 and RABEP1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 197 FT /note="I->A: Abolishes interaction with ARF1, UBC and FT TSG101." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 198 FT /note="K->A: Abolishes interaction with ARF1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 200 FT /note="M->A: Abolishes interaction with ARF1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 204 FT /note="D->A: Abolishes interaction with ARF1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 259 FT /note="M->K: Abolishes interaction with RABEP1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 260 FT /note="R->A: No effect on interaction with RABEP1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 260 FT /note="R->E: Abolishes interaction with RABEP1 and UBC." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 264 FT /note="F->A: Abolishes interaction with RABEP1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 267 FT /note="A->D: Abolishes interaction with RABEP1 and UBC." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 277 FT /note="L->A: Abolishes interaction with RABEP1, UBC and FT TSG101." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 281 FT /note="L->A: Abolishes interaction with RABEP1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 284 FT /note="N->A: Abolishes interaction with RABEP1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 284 FT /note="N->S: Abolishes interaction with RABEP1." FT /evidence="ECO:0000269|PubMed:15143060" FT MUTAGEN 355 FT /note="S->A: Increased interaction with IGF2R. Reduced FT phosphorylation. No effect on the interaction with SORL1." FT /evidence="ECO:0000269|PubMed:12060753, FT ECO:0000269|PubMed:20015111" FT MUTAGEN 355 FT /note="S->D: Abolishes interaction with IGF2R. No effect on FT the interaction with SORL1." FT /evidence="ECO:0000269|PubMed:12060753, FT ECO:0000269|PubMed:20015111" FT MUTAGEN 356..360 FT /note="LLDDE->AADAA: Partial loss of clathrin-binding." FT /evidence="ECO:0000269|PubMed:11301005" FT MUTAGEN 358 FT /note="D->A: Increased interaction with IGF2R." FT /evidence="ECO:0000269|PubMed:12060753" FT MUTAGEN 361..362 FT /note="LM->AA: Increased interaction with IGF2R." FT /evidence="ECO:0000269|PubMed:12060753" FT MUTAGEN 563 FT /note="A->D: Abolishes interaction with CCDC91." FT /evidence="ECO:0000269|PubMed:12808037" FT MUTAGEN 564 FT /note="V->D: Abolishes interaction with CCDC91." FT /evidence="ECO:0000269|PubMed:12808037" FT MUTAGEN 570 FT /note="V->E: Abolishes interaction with CCDC91." FT /evidence="ECO:0000269|PubMed:12808037" FT MUTAGEN 572 FT /note="L->E: Abolishes interaction with CCDC91." FT /evidence="ECO:0000269|PubMed:12808037" FT HELIX 3..5 FT /evidence="ECO:0007829|PDB:1UJK" FT HELIX 10..17 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 27..36 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:3G2S" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 43..55 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 60..76 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 79..85 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 88..98 FT /evidence="ECO:0007829|PDB:3G2S" FT TURN 100..103 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 109..125 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 130..141 FT /evidence="ECO:0007829|PDB:3G2S" FT HELIX 172..182 FT /evidence="ECO:0007829|PDB:1J2J" FT HELIX 187..205 FT /evidence="ECO:0007829|PDB:1J2J" FT HELIX 212..233 FT /evidence="ECO:0007829|PDB:1X79" FT TURN 235..238 FT /evidence="ECO:0007829|PDB:1O3X" FT HELIX 243..267 FT /evidence="ECO:0007829|PDB:1O3X" FT HELIX 274..298 FT /evidence="ECO:0007829|PDB:1O3X" FT HELIX 494..497 FT /evidence="ECO:0007829|PDB:1NA8" FT HELIX 504..506 FT /evidence="ECO:0007829|PDB:1NA8" FT STRAND 515..520 FT /evidence="ECO:0007829|PDB:1NA8" FT STRAND 523..531 FT /evidence="ECO:0007829|PDB:1NA8" FT STRAND 533..535 FT /evidence="ECO:0007829|PDB:2DWY" FT STRAND 540..549 FT /evidence="ECO:0007829|PDB:1NA8" FT STRAND 555..563 FT /evidence="ECO:0007829|PDB:1NA8" FT STRAND 568..572 FT /evidence="ECO:0007829|PDB:1NA8" FT STRAND 592..599 FT /evidence="ECO:0007829|PDB:1NA8" FT STRAND 608..616 FT /evidence="ECO:0007829|PDB:1NA8" FT STRAND 619..627 FT /evidence="ECO:0007829|PDB:1NA8" FT TURN 633..635 FT /evidence="ECO:0007829|PDB:1NA8" FT HELIX 636..638 FT /evidence="ECO:0007829|PDB:1NA8" SQ SEQUENCE 639 AA; 70384 MW; B0B6F089FA0F7DD5 CRC64; MEPAMEPETL EARINRATNP LNKELDWASI NGFCEQLNED FEGPPLATRL LAHKIQSPQE WEAIQALTVL ETCMKSCGKR FHDEVGKFRF LNELIKVVSP KYLGSRTSEK VKNKILELLY SWTVGLPEEV KIAEAYQMLK KQGIVKSDPK LPDDTTFPLP PPRPKNVIFE DEEKSKMLAR LLKSSHPEDL RAANKLIKEM VQEDQKRMEK ISKRVNAIEE VNNNVKLLTE MVMSHSQGGA AAGSSEDLMK ELYQRCERMR PTLFRLASDT EDNDEALAEI LQANDNLTQV INLYKQLVRG EEVNGDATAG SIPGSTSALL DLSGLDLPPA GTTYPAMPTR PGEQASPEQP SASVSLLDDE LMSLGLSDPT PPSGPSLDGT GWNSFQSSDA TEPPAPALAQ APSMESRPPA QTSLPASSGL DDLDLLGKTL LQQSLPPESQ QVRWEKQQPT PRLTLRDLQN KSSSCSSPSS SATSLLHTVS PEPPRPPQQP VPTELSLASI TVPLESIKPS NILPVTVYDQ HGFRILFHFA RDPLPGRSDV LVVVVSMLST APQPIRNIVF QSAVPKVMKV KLQPPSGTEL PAFNPIVHPS AITQVLLLAN PQKEKVRLRY KLTFTMGDQT YNEMGDVDQF PPPETWGSL //